ACDC_BACSU
ID ACDC_BACSU Reviewed; 380 AA.
AC O34421; Q799L4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable acyl-CoA dehydrogenase YngJ;
DE EC=1.3.99.-;
GN Name=yngJ; OrderedLocusNames=BSU18260;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387222; DOI=10.1099/00221287-143-11-3443;
RA Tosato V., Albertini A.M., Zotti M., Sonda S., Bruschi C.V.;
RT "Sequence completion, identification and definition of the fengycin operon
RT in Bacillus subtilis 168.";
RL Microbiology 143:3443-3450(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a 2,3-saturated acyl-CoA = a 2,3-dehydroacyl-CoA + AH2;
CC Xref=Rhea:RHEA:48608, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:60015, ChEBI:CHEBI:65111;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; Y13917; CAA74221.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13709.1; -; Genomic_DNA.
DR PIR; G69893; G69893.
DR RefSeq; NP_389708.1; NC_000964.3.
DR RefSeq; WP_003245114.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34421; -.
DR SMR; O34421; -.
DR STRING; 224308.BSU18260; -.
DR PaxDb; O34421; -.
DR PRIDE; O34421; -.
DR EnsemblBacteria; CAB13709; CAB13709; BSU_18260.
DR GeneID; 939996; -.
DR KEGG; bsu:BSU18260; -.
DR PATRIC; fig|224308.179.peg.1992; -.
DR eggNOG; COG1960; Bacteria.
DR InParanoid; O34421; -.
DR OMA; AMEELFW; -.
DR PhylomeDB; O34421; -.
DR BioCyc; BSUB:BSU18260-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..380
FT /note="Probable acyl-CoA dehydrogenase YngJ"
FT /id="PRO_0000380229"
FT ACT_SITE 364
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 123..132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 156..158
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 337..341
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 366..368
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 40919 MW; 6887A0EF1CF1882B CRC64;
MNFELTKEQQ MVREMVKDFA KKEIAPHAEH VDQTGEFPMQ TFKKMGELGL MGIPFPEEYG
GSGGDTISYA LAVEEVGKAC GSTGLSYAAA VSLGASPLYY FGTEEQKQTH LTPLASGTAL
GSFGLTEPNA GSDAGGTQTK AISNGDEYVI NGEKCWITNA SYARTVIVTA VTGKNKDGKN
IISALIVPTD TPGLTITSPY DKMGVRGSNT AEILLEDVRV PAANLLGDPT KGFKQFLYTL
DGGRISIAAL AVGIAQAALD ASLAYAKERK QFGQPISSFQ AIQFKLADMA MEIDLARQMV
LKAAWLKDHN RPFTKEAAYA KLFASEMATR ACNQAIQIHG GSGYMKEYGV ERMLRDAKLM
EIGEGTSEIQ RLVIARQLLK
